{"technology":{"slug":"protein-structure","name":"Protein Structure Prediction","description":"Computational protein biology. AlphaFold, protein design, structure prediction, drug discovery through molecular simulation, and de novo protein engineering.","discipline":"Biochemistry / AI","icon":"🔬"},"lastUpdated":"2026-07-21T06:27:46.858Z","articleCount":15,"articles":[{"id":"oa-W3177828909","title":"Highly accurate protein structure prediction with AlphaFold","authors":"John Jumper, Richard Evans, Alexander Pritzel, Tim Green, Michael Figurnov, Olaf Ronneberger, Kathryn Tunyasuvunakool, Russ Bates, Augustin Žídek, Anna Potapenko, Alex Bridgland, Clemens Meyer, Simon Köhl, Andrew J. Ballard, Andrew Cowie, Bernardino Romera‐Paredes, Stanislav Nikolov, Rishub Jain, Jonas Adler, Trevor Back, Stig Petersen, David Reiman, Ellen Clancy, Michał Zieliński, Martin Steinegger, Michalina Pacholska, Tamas Berghammer, Sebastian W. Bodenstein, David Silver, Oriol Vinyals, Andrew Senior, Koray Kavukcuoglu, Pushmeet Kohli, Demis Hassabis","journal":"Nature","pubDate":"2021-07-15","doi":"10.1038/s41586-021-03819-2","abstract":"Abstract Proteins are essential to life, and understanding their structure can facilitate a mechanistic understanding of their function. Through an enormous experimental effort 1–4 , the structures of around 100,000 unique proteins have been determined 5 , but this represents a small fraction of the billions of known protein sequences 6,7 . Structural coverage is bottlenecked by the months to years of painstaking effort required to determine a single protein structure. Accurate computational approaches are needed to address this gap and to enable large-scale structural bioinformatics. Predicting the three-dimensional structure that a protein will adopt based solely on its amino acid sequence—the structure prediction component of the ‘protein folding problem’ 8 —has been an important open research problem for more than 50 years 9 . Despite recent progress 10–14 , existing methods fall far short of atomic accuracy, especially when no homologous structure is available. Here we provide the first computational method that can regularly predict protein structures with atomic accuracy even in cases in which no similar structure is known. We validated an entirely redesigned version of our neural network-based model, AlphaFold, in the challenging 14th Critical Assessment of protein Structure Prediction (CASP14) 15 , demonstrating accuracy competitive with experimental structures in a majority of cases and greatly outperforming other methods. Underpinning the latest version of AlphaFold is a novel machine learning approach that incorporates physical and biological knowledge about protein structure, leveraging multi-sequence alignments, into the design of the deep learning algorithm.","tldr":"","source":"OpenAlex","sourceUrl":"https://openalex.org/W3177828909","citationCount":45812,"isOpenAccess":true,"pdfUrl":"https://www.nature.com/articles/s41586-021-03819-2.pdf"},{"id":"oa-W4396721167","title":"Accurate structure prediction of biomolecular interactions with AlphaFold 3","authors":"Josh Abramson, Jonas Adler, Jack Dunger, Richard Evans, Tim Green, Alexander Pritzel, Olaf Ronneberger, Lindsay Willmore, Andrew J. Ballard, Joshua Bambrick, Sebastian W. Bodenstein, David A. Evans, Chia-Chun Hung, Michael O’Neill, David Reiman, Kathryn Tunyasuvunakool, Zachary Wu, Akvilė Žemgulytė, Eirini Arvaniti, Charles Beattie, Ottavia Bertolli, Alex Bridgland, Alexey V. Cherepanov, Miles Congreve, Alexander I. Cowen-Rivers, Andrew Cowie, Michael Figurnov, Fabian B. Fuchs, Hannah Gladman, Rishub Jain, Yousuf A. Khan, Caroline M. R. Low, Kuba Perlin, Anna Potapenko, Pascal Savy, Sukhdeep Singh, Adrian Stecuła, Ashok Thillaisundaram, Catherine Tong, Sergei Yakneen, Ellen D. Zhong, Michał Zieliński, Augustin Žídek, Victor Bapst, Pushmeet Kohli, Max Jaderberg, Demis Hassabis, John Jumper","journal":"Nature","pubDate":"2024-05-08","doi":"10.1038/s41586-024-07487-w","abstract":"Abstract The introduction of AlphaFold 2 1 has spurred a revolution in modelling the structure of proteins and their interactions, enabling a huge range of applications in protein modelling and design 2–6 . Here we describe our AlphaFold 3 model with a substantially updated diffusion-based architecture that is capable of predicting the joint structure of complexes including proteins, nucleic acids, small molecules, ions and modified residues. The new AlphaFold model demonstrates substantially improved accuracy over many previous specialized tools: far greater accuracy for protein–ligand interactions compared with state-of-the-art docking tools, much higher accuracy for protein–nucleic acid interactions compared with nucleic-acid-specific predictors and substantially higher antibody–antigen prediction accuracy compared with AlphaFold-Multimer v.2.3 7,8 . Together, these results show that high-accuracy modelling across biomolecular space is possible within a single unified deep-learning framework.","tldr":"","source":"OpenAlex","sourceUrl":"https://openalex.org/W4396721167","citationCount":14375,"isOpenAccess":true,"pdfUrl":"https://www.nature.com/articles/s41586-024-07487-w_reference.pdf"},{"id":"oa-W4281790889","title":"ColabFold: making protein folding accessible to all","authors":"Milot Mirdita, Konstantin Schütze, Yoshitaka Moriwaki, Lim Heo, Sergey Ovchinnikov, Martin Steinegger","journal":"Nature Methods","pubDate":"2022-05-30","doi":"10.1038/s41592-022-01488-1","abstract":"ColabFold offers accelerated prediction of protein structures and complexes by combining the fast homology search of MMseqs2 with AlphaFold2 or RoseTTAFold. ColabFold's 40-60-fold faster search and optimized model utilization enables prediction of close to 1,000 structures per day on a server with one graphics processing unit. Coupled with Google Colaboratory, ColabFold becomes a free and accessible platform for protein folding. ColabFold is open-source software available at https://github.com/sokrypton/ColabFold and its novel environmental databases are available at https://colabfold.mmseqs.com .","tldr":"","source":"OpenAlex","sourceUrl":"https://openalex.org/W4281790889","citationCount":9813,"isOpenAccess":true,"pdfUrl":"https://www.nature.com/articles/s41592-022-01488-1.pdf"},{"id":"oa-W4308834893","title":"The STRING database in 2023: protein–protein association networks and functional enrichment analyses for any sequenced genome of interest","authors":"Damian Szklarczyk, Rebecca Kirsch, Mikaela Koutrouli, Katerina Nastou, Farrokh Mehryary, Radja Hachilif, Annika L. Gable, Tao Fang, Nadezhda T. Doncheva, Sampo Pyysalo, Peer Bork, Lars Juhl Jensen, Christian von Mering","journal":"Nucleic Acids Research","pubDate":"2022-11-12","doi":"10.1093/nar/gkac1000","abstract":"Much of the complexity within cells arises from functional and regulatory interactions among proteins. The core of these interactions is increasingly known, but novel interactions continue to be discovered, and the information remains scattered across different database resources, experimental modalities and levels of mechanistic detail. The STRING database (https://string-db.org/) systematically collects and integrates protein-protein interactions-both physical interactions as well as functional associations. The data originate from a number of sources: automated text mining of the scientific literature, computational interaction predictions from co-expression, conserved genomic context, databases of interaction experiments and known complexes/pathways from curated sources. All of these interactions are critically assessed, scored, and subsequently automatically transferred to less well-studied organisms using hierarchical orthology information. The data can be accessed via the website, but also programmatically and via bulk downloads. The most recent developments in STRING (version 12.0) are: (i) it is now possible to create, browse and analyze a full interaction network for any novel genome of interest, by submitting its complement of encoded proteins, (ii) the co-expression channel now uses variational auto-encoders to predict interactions, and it covers two new sources, single-cell RNA-seq and experimental proteomics data and (iii) the confidence in each experimentally derived interaction is now estimated based on the detection method used, and communicated to the user in the web-interface. Furthermore, STRING continues to enhance its facilities for functional enrichment analysis, which are now fully available also for user-submitted genomes.","tldr":"","source":"OpenAlex","sourceUrl":"https://openalex.org/W4308834893","citationCount":9036,"isOpenAccess":true,"pdfUrl":"https://academic.oup.com/nar/article-pdf/51/D1/D638/48440966/gkac1000.pdf"},{"id":"oa-W3211795435","title":"AlphaFold Protein Structure Database: massively expanding the structural coverage of protein-sequence space with high-accuracy models","authors":"Mihály Váradi, Stephen Anyango, Mandar Deshpande, Sreenath Nair, Cindy Natassia, Galabina Yordanova, David Yu Yuan, Oana Stroe, Gemma Wood, Agata Laydon, Augustin Žídek, Tim Green, Kathryn Tunyasuvunakool, Stig Petersen, John Jumper, Ellen Clancy, Richard Green, Ankur Vora, Mira Lutfi, Michael Figurnov, Andrew Cowie, Nicole Hobbs, Pushmeet Kohli, Gerard J. Kleywegt, Ewan Birney, Demis Hassabis, Sameer Velankar","journal":"Nucleic Acids Research","pubDate":"2021-10-19","doi":"10.1093/nar/gkab1061","abstract":"The AlphaFold Protein Structure Database (AlphaFold DB, https://alphafold.ebi.ac.uk) is an openly accessible, extensive database of high-accuracy protein-structure predictions. Powered by AlphaFold v2.0 of DeepMind, it has enabled an unprecedented expansion of the structural coverage of the known protein-sequence space. AlphaFold DB provides programmatic access to and interactive visualization of predicted atomic coordinates, per-residue and pairwise model-confidence estimates and predicted aligned errors. The initial release of AlphaFold DB contains over 360,000 predicted structures across 21 model-organism proteomes, which will soon be expanded to cover most of the (over 100 million) representative sequences from the UniRef90 data set.","tldr":"","source":"OpenAlex","sourceUrl":"https://openalex.org/W3211795435","citationCount":8368,"isOpenAccess":true,"pdfUrl":"https://doi.org/10.1093/nar/gkab1061"},{"id":"oa-W3186179742","title":"Accurate prediction of protein structures and interactions using a three-track neural network","authors":"Minkyung Baek, Frank DiMaio, Ivan Anishchenko, Justas Dauparas, Sergey Ovchinnikov, Gyu Rie Lee, Jue Wang, Qian Cong, Lisa N. Kinch, R. Dustin Schaeffer, Claudia Millán, Hahnbeom Park, Carson Adams, Caleb R. Glassman, Andy DeGiovanni, J.H. Pereira, Andria V. Rodrigues, Alberdina A. van Dijk, Ana C. Ebrecht, Diederik J. Opperman, Theo Sagmeister, Christoph Buhlheller, Tea Pavkov‐Keller, Manoj Kumar Rathinaswamy, Udit Dalwadi, Calvin K. Yip, John E. Burke, K. Christopher García, Nick V. Grishin, Paul D. Adams, Randy J. Read, David Baker","journal":"Science","pubDate":"2021-07-15","doi":"10.1126/science.abj8754","abstract":"DeepMind presented notably accurate predictions at the recent 14th Critical Assessment of Structure Prediction (CASP14) conference. We explored network architectures that incorporate related ideas and obtained the best performance with a three-track network in which information at the one-dimensional (1D) sequence level, the 2D distance map level, and the 3D coordinate level is successively transformed and integrated. The three-track network produces structure predictions with accuracies approaching those of DeepMind in CASP14, enables the rapid solution of challenging x-ray crystallography and cryo-electron microscopy structure modeling problems, and provides insights into the functions of proteins of currently unknown structure. The network also enables rapid generation of accurate protein-protein complex models from sequence information alone, short-circuiting traditional approaches that require modeling of individual subunits followed by docking. We make the method available to the scientific community to speed biological research.","tldr":"","source":"OpenAlex","sourceUrl":"https://openalex.org/W3186179742","citationCount":5781,"isOpenAccess":true,"pdfUrl":"https://escholarship.org/content/qt3gz3w9v7/qt3gz3w9v7.pdf?t=rfdtpb"},{"id":"oa-W3202105508","title":"Protein complex prediction with AlphaFold-Multimer","authors":"Richard Evans, M. E. O’Neill, Alexander Pritzel, Н. В. Антропова, Andrew Senior, Tim Green, Augustin Žídek, Russ Bates, Sam Blackwell, Jason Yim, Olaf Ronneberger, Sebastian W. Bodenstein, Michał Zieliński, Alex Bridgland, Anna Potapenko, Andrew Cowie, Kathryn Tunyasuvunakool, Rishub Jain, Ellen Clancy, Pushmeet Kohli, John Jumper, Demis Hassabis","journal":"bioRxiv (Cold Spring Harbor Laboratory)","pubDate":"2021-10-04","doi":"10.1101/2021.10.04.463034","abstract":"While the vast majority of well-structured single protein chains can now be predicted to high accuracy due to the recent AlphaFold [1] model, the prediction of multi-chain protein complexes remains a challenge in many cases. In this work, we demonstrate that an AlphaFold model trained specifically for multimeric inputs of known stoichiometry, which we call AlphaFold-Multimer, significantly increases accuracy of predicted multimeric interfaces over input-adapted single-chain AlphaFold while maintaining high intra-chain accuracy. On a benchmark dataset of 17 heterodimer proteins without templates (introduced in [2]) we achieve at least medium accuracy (DockQ [3] ≥ 0.49) on 13 targets and high accuracy (DockQ ≥ 0.8) on 7 targets, compared to 9 targets of at least medium accuracy and 4 of high accuracy for the previous state of the art system (an AlphaFold-based system from [2]). We also predict structures for a large dataset of 4,446 recent protein complexes, from which we score all non-redundant interfaces with low template identity. For heteromeric interfaces we successfully predict the interface (DockQ ≥ 0.23) in 70% of cases, and produce high accuracy predictions (DockQ ≥ 0.8) in 26% of cases, an improvement of +27 and +14 percentage points over the flexible linker modification of AlphaFold [4] respectively. For homomeric inter-faces we successfully predict the interface in 72% of cases, and produce high accuracy predictions in 36% of cases, an improvement of +8 and +7 percentage points respectively.","tldr":"","source":"OpenAlex","sourceUrl":"https://openalex.org/W3202105508","citationCount":4095,"isOpenAccess":false,"pdfUrl":""},{"id":"oa-W2999044305","title":"Improved protein structure prediction using potentials from deep learning","authors":"Andrew Senior, Richard Evans, John Jumper, James Kirkpatrick, Laurent Sifre, Tim Green, Chongli Qin, Augustin Žídek, Alexander Nelson, Alex Bridgland, Hugo Penedones, Stig Petersen, Karen Simonyan, Steve Crossan, Pushmeet Kohli, David T. Jones, David Silver, Koray Kavukcuoglu, Demis Hassabis","journal":"Nature","pubDate":"2020-01-15","doi":"10.1038/s41586-019-1923-7","abstract":"","tldr":"","source":"OpenAlex","sourceUrl":"https://openalex.org/W2999044305","citationCount":3551,"isOpenAccess":true,"pdfUrl":"https://discovery.ucl.ac.uk/10089234/1/343019_3_art_0_py4t4l_convrt.pdf"},{"id":"oa-W3183475563","title":"Highly accurate protein structure prediction for the human proteome","authors":"Kathryn Tunyasuvunakool, Jonas Adler, Zachary Wu, Tim Green, Michał Zieliński, Augustin Žídek, Alex Bridgland, Andrew Cowie, Clemens Meyer, Agata Laydon, Sameer Velankar, Gerard J. Kleywegt, Alex Bateman, Richard Evans, Alexander Pritzel, Michael Figurnov, Olaf Ronneberger, Russ Bates, Simon Köhl, Anna Potapenko, Andrew J. Ballard, Bernardino Romera‐Paredes, Stanislav Nikolov, Rishub Jain, Ellen Clancy, David Reiman, Stig Petersen, Andrew Senior, Koray Kavukcuoglu, Ewan Birney, Pushmeet Kohli, John Jumper, Demis Hassabis","journal":"Nature","pubDate":"2021-07-22","doi":"10.1038/s41586-021-03828-1","abstract":"Abstract Protein structures can provide invaluable information, both for reasoning about biological processes and for enabling interventions such as structure-based drug development or targeted mutagenesis. After decades of effort, 17% of the total residues in human protein sequences are covered by an experimentally determined structure 1 . Here we markedly expand the structural coverage of the proteome by applying the state-of-the-art machine learning method, AlphaFold 2 , at a scale that covers almost the entire human proteome (98.5% of human proteins). The resulting dataset covers 58% of residues with a confident prediction, of which a subset (36% of all residues) have very high confidence. We introduce several metrics developed by building on the AlphaFold model and use them to interpret the dataset, identifying strong multi-domain predictions as well as regions that are likely to be disordered. Finally, we provide some case studies to illustrate how high-quality predictions could be used to generate biological hypotheses. We are making our predictions freely available to the community and anticipate that routine large-scale and high-accuracy structure prediction will become an important tool that will allow new questions to be addressed from a structural perspective.","tldr":"","source":"OpenAlex","sourceUrl":"https://openalex.org/W3183475563","citationCount":3249,"isOpenAccess":true,"pdfUrl":"https://www.nature.com/articles/s41586-021-03828-1.pdf"},{"id":"oa-W4388464011","title":"AlphaFold Protein Structure Database in 2024: providing structure coverage for over 214 million protein sequences","authors":"Mihály Váradi, Damian Bertoni, Paulyna Magaña, Urmila Paramval, Ivanna Pidruchna, Malarvizhi Radhakrishnan, Maxim Tsenkov, Sreenath Nair, Milot Mirdita, Jingi Yeo, Oleg Kovalevskiy, Kathryn Tunyasuvunakool, Agata Laydon, Augustin Žídek, Hamish Tomlinson, Dhavanthi Hariharan, Josh Abrahamson, Tim Green, John Jumper, Ewan Birney, Martin Steinegger, Demis Hassabis, Sameer Velankar","journal":"Nucleic Acids Research","pubDate":"2023-11-02","doi":"10.1093/nar/gkad1011","abstract":"The AlphaFold Database Protein Structure Database (AlphaFold DB, https://alphafold.ebi.ac.uk) has significantly impacted structural biology by amassing over 214 million predicted protein structures, expanding from the initial 300k structures released in 2021. Enabled by the groundbreaking AlphaFold2 artificial intelligence (AI) system, the predictions archived in AlphaFold DB have been integrated into primary data resources such as PDB, UniProt, Ensembl, InterPro and MobiDB. Our manuscript details subsequent enhancements in data archiving, covering successive releases encompassing model organisms, global health proteomes, Swiss-Prot integration, and a host of curated protein datasets. We detail the data access mechanisms of AlphaFold DB, from direct file access via FTP to advanced queries using Google Cloud Public Datasets and the programmatic access endpoints of the database. We also discuss the improvements and services added since its initial release, including enhancements to the Predicted Aligned Error viewer, customisation options for the 3D viewer, and improvements in the search engine of AlphaFold DB.","tldr":"","source":"OpenAlex","sourceUrl":"https://openalex.org/W4388464011","citationCount":1991,"isOpenAccess":true,"pdfUrl":"https://academic.oup.com/nar/advance-article-pdf/doi/10.1093/nar/gkad1011/52777135/gkad1011.pdf"},{"id":"oa-W4296032638","title":"Robust deep learning–based protein sequence design using ProteinMPNN","authors":"Justas Dauparas, Ivan Anishchenko, Nathaniel R. Bennett, Hua Bai, Robert J. Ragotte, Lukas F. Milles, Basile I. M. Wicky, Alexis Courbet, Robbert J. de Haas, Neville P. Bethel, Philip J. Y. Leung, Timothy F. Huddy, Samuel J. Pellock, Doug Tischer, F. Chan, Brian Koepnick, Hannah Nguyen, Alex Kang, Banumathi Sankaran, Asim K. Bera, Neil P. King, David Baker","journal":"Science","pubDate":"2022-09-15","doi":"10.1126/science.add2187","abstract":"Although deep learning has revolutionized protein structure prediction, almost all experimentally characterized de novo protein designs have been generated using physically based approaches such as Rosetta. Here, we describe a deep learning-based protein sequence design method, ProteinMPNN, that has outstanding performance in both in silico and experimental tests. On native protein backbones, ProteinMPNN has a sequence recovery of 52.4% compared with 32.9% for Rosetta. The amino acid sequence at different positions can be coupled between single or multiple chains, enabling application to a wide range of current protein design challenges. We demonstrate the broad utility and high accuracy of ProteinMPNN using x-ray crystallography, cryo-electron microscopy, and functional studies by rescuing previously failed designs, which were made using Rosetta or AlphaFold, of protein monomers, cyclic homo-oligomers, tetrahedral nanoparticles, and target-binding proteins.","tldr":"","source":"OpenAlex","sourceUrl":"https://openalex.org/W4296032638","citationCount":1913,"isOpenAccess":true,"pdfUrl":"https://www.osti.gov/servlets/purl/2470608"},{"id":"oa-W2997234557","title":"Improved protein structure prediction using predicted interresidue orientations","authors":"Jianyi Yang, Ivan Anishchenko, Hahnbeom Park, Zhenling Peng, Sergey Ovchinnikov, David Baker","journal":"Proceedings of the National Academy of Sciences","pubDate":"2020-01-02","doi":"10.1073/pnas.1914677117","abstract":"The prediction of interresidue contacts and distances from coevolutionary data using deep learning has considerably advanced protein structure prediction. Here, we build on these advances by developing a deep residual network for predicting interresidue orientations, in addition to distances, and a Rosetta-constrained energy-minimization protocol for rapidly and accurately generating structure models guided by these restraints. In benchmark tests on 13th Community-Wide Experiment on the Critical Assessment of Techniques for Protein Structure Prediction (CASP13)- and Continuous Automated Model Evaluation (CAMEO)-derived sets, the method outperforms all previously described structure-prediction methods. Although trained entirely on native proteins, the network consistently assigns higher probability to de novo-designed proteins, identifying the key fold-determining residues and providing an independent quantitative measure of the \"ideality\" of a protein structure. The method promises to be useful for a broad range of protein structure prediction and design problems.","tldr":"","source":"OpenAlex","sourceUrl":"https://openalex.org/W2997234557","citationCount":1568,"isOpenAccess":true,"pdfUrl":"https://www.pnas.org/doi/pdf/10.1073/pnas.1914677117"},{"id":"oa-W3195375135","title":"AlphaFold and Implications for Intrinsically Disordered Proteins","authors":"Kiersten M. Ruff, Rohit V. Pappu","journal":"Journal of Molecular Biology","pubDate":"2021-08-18","doi":"10.1016/j.jmb.2021.167208","abstract":"Accurate predictions of the three-dimensional structures of proteins from their amino acid sequences have come of age. AlphaFold, a deep learning-based approach to protein structure prediction, shows remarkable success in independent assessments of prediction accuracy. A significant epoch in structural bioinformatics was the structural annotation of over 98% of protein sequences in the human proteome. Interestingly, many predictions feature regions of very low confidence, and these regions largely overlap with intrinsically disordered regions (IDRs). That over 30% of regions within the proteome are disordered is congruent with estimates that have been made over the past two decades, as intense efforts have been undertaken to generalize the structure-function paradigm to include the importance of conformational heterogeneity and dynamics. With structural annotations from AlphaFold in hand, there is the temptation to draw inferences regarding the \"structures\" of IDRs and their interactomes. Here, we offer a cautionary note regarding the misinterpretations that might ensue and highlight efforts that provide concrete understanding of sequence-ensemble-function relationships of IDRs. This perspective is intended to emphasize the importance of IDRs in sequence-function relationships (SERs) and to highlight how one might go about extracting quantitative SERs to make sense of how IDRs function.","tldr":"","source":"OpenAlex","sourceUrl":"https://openalex.org/W3195375135","citationCount":676,"isOpenAccess":true,"pdfUrl":"https://doi.org/10.1016/j.jmb.2021.167208"},{"id":"oa-W4206563428","title":"Protein structure predictions to atomic accuracy with AlphaFold","authors":"John Jumper, Demis Hassabis","journal":"Nature Methods","pubDate":"2022-01-01","doi":"10.1038/s41592-021-01362-6","abstract":"","tldr":"","source":"OpenAlex","sourceUrl":"https://openalex.org/W4206563428","citationCount":293,"isOpenAccess":false,"pdfUrl":""},{"id":"oa-W2967175367","title":"Protein structure prediction beyond AlphaFold","authors":"Guo‐Wei Wei","journal":"Nature Machine Intelligence","pubDate":"2019-08-09","doi":"10.1038/s42256-019-0086-4","abstract":"","tldr":"","source":"OpenAlex","sourceUrl":"https://openalex.org/W2967175367","citationCount":85,"isOpenAccess":true,"pdfUrl":"https://pmc.ncbi.nlm.nih.gov/articles/PMC10956386/pdf/nihms-1972073.pdf"}],"links":{"web":"https://science-database.com/technology/protein-structure","llms_txt":"https://science-database.com/technology/protein-structure/llms.txt","api":"https://science-database.com/api/v1/technology/protein-structure"}}